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Issue 15, 2013
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Enzyme immobilisation in biocatalysis: why, what and how

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Abstract

In this tutorial review, an overview of the why, what and how of enzyme immobilisation for use in biocatalysis is presented. The importance of biocatalysis in the context of green and sustainable chemicals manufacture is discussed and the necessity for immobilisation of enzymes as a key enabling technology for practical and commercial viability is emphasised. The underlying reasons for immobilisation are the need to improve the stability and recyclability of the biocatalyst compared to the free enzyme. The lower risk of product contamination with enzyme residues and low or no allergenicity are further advantages of immobilised enzymes. Methods for immobilisation are divided into three categories: adsorption on a carrier (support), encapsulation in a carrier, and cross-linking (carrier-free). General considerations regarding immobilisation, regardless of the method used, are immobilisation yield, immobilisation efficiency, activity recovery, enzyme loading (wt% in the biocatalyst) and the physical properties, e.g. particle size and density, hydrophobicity and mechanical robustness of the immobilisate, i.e. the immobilised enzyme as a whole (enzyme + support). The choice of immobilisate is also strongly dependent on the reactor configuration used, e.g. stirred tank, fixed bed, fluidised bed, and the mode of downstream processing. Emphasis is placed on relatively recent developments, such as the use of novel supports such as mesoporous silicas, hydrogels, and smart polymers, and cross-linked enzyme aggregates (CLEAs).

Graphical abstract: Enzyme immobilisation in biocatalysis: why, what and how

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Publication details

The article was received on 24 Feb 2013 and first published on 27 Mar 2013


Article type: Tutorial Review
DOI: 10.1039/C3CS60075K
Chem. Soc. Rev., 2013,42, 6223-6235
  • Open access: Creative Commons BY license
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    Enzyme immobilisation in biocatalysis: why, what and how

    R. A. Sheldon and S. van Pelt, Chem. Soc. Rev., 2013, 42, 6223
    DOI: 10.1039/C3CS60075K

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